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Chromatin Immunoprecipitation- ChIP

Chromatin Immunoprecipitation- ChIP

Chromatin immunoprecipitation, or ChIP, is an antibody-based technique used to identify sites on DNA that bind to transcription factors of interest or histone proteins. It also helps determine the type of histone modifications such as acetylation, phosphorylation, or methylation.
Types of ChIP
ChIP can be divided into two types - X-ChIP and N-ChIP. X-ChIP involves in vivo cross-linking of histones and regulatory proteins to DNA, fragmenting the DNA by sonication, and isolating the protein-DNA...

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Related Experiment Video

Updated: Oct 6, 2025

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays.

Ruchir C Bobde¹, Ketul Saharan¹, Somanath Baral²

¹Institute of Life Sciences; Regional Centre for Biotechnology.

Journal of Visualized Experiments : Jove

|January 17, 2022

Summary

This study presents a protocol using in vitro techniques to identify histone chaperones, proteins crucial for nucleosome assembly. These methods help confirm a protein's function in shuttling histones and aiding DNA deposition.

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Last Updated: Oct 6, 2025

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Sequential Salt Extractions for the Analysis of Bulk Chromatin Binding Properties of Chromatin Modifying Complexes

Sequential Salt Extractions for the Analysis of Bulk Chromatin Binding Properties of Chromatin Modifying Complexes

Published on: October 2, 2017

Area of Science:

Molecular Biology
Biochemistry
Cell Biology

Background:

Chromatin, the complex of DNA and proteins in eukaryotes, is fundamental for genome organization.
Nucleosomes, the basic units of chromatin, are assembled by core histones (H2A, H2B, H3, H4) and DNA.
Histone chaperones are essential proteins that facilitate histone transport and deposition during nucleosome assembly.

Purpose of the Study:

To describe a standardized protocol for identifying and confirming the function of histone chaperone proteins.
To provide researchers with a reliable method for characterizing novel histone-binding proteins.

Main Methods:

Utilizing a combination of in vitro laboratory techniques.
Employing pull-down assays to assess protein interactions.
Applying analytical size-exclusion chromatography and analytical ultra-centrifugation for biophysical characterization.
Implementing a histone chaperoning assay to functionally validate protein activity.

Main Results:

The described tandem assays provide a comprehensive approach to verify histone chaperone activity.
The protocol allows for the differentiation of specific histone chaperone functions (e.g., H2A/H2B vs. H3/H4).

Conclusions:

This protocol offers a robust framework for the functional characterization of histone chaperones.
Accurate identification of histone chaperones is critical for understanding nucleosome assembly and chromatin dynamics.